Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans

R. J. Lye, M. E. Porter, J. M. Scholey, J. R. McIntosh

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138 Scopus citations


C. elegans contains a microtubule binding protein that resembles both dynein and kinesin. This protein has a MgATPase activity and copurifies on both sucrose gradients and DEAE Sephadex columns with a polypeptide of Mr approximately 400 kd. The ATPase activity is 50% inhibited by 10 μM vanadate, 1 mM N-ethyl maleimide, or 5 mM AMP-PNP; it is enhanced 50% by 0.2% Triton. The 400 kd polypeptide is cleaved at a single site by ultraviolet light in the presence of ATP and vanadate. In these ways, the protein resembles dynein. The protein also promotes ATP-dependent translocation of microtubules or axonemes, "plus" ends trailing. This property is kinesin-like; however, the motility is blocked by 5 μM vanadate, 1 mM N-ethyl maleimide, 0.5 mM ATP-γ-S, or by ATP-vanadate-UV cleavage of the 400 kd polypeptide, characteristics that differ from kinesin. We propose that this protein is a novel microtubule translocator.

Original languageEnglish (US)
Pages (from-to)309-318
Number of pages10
Issue number2
StatePublished - Oct 23 1987
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology


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